Analytical Data
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Gene name
GYPA
- Application
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Alternative Names
CD235a; MN; MNS; GPA; GPErik; GPSAT; PAS-2; GpMiIII; HGpMiIII; HGpMiV; HGpMiX; HGpMiXI; HGpSta; Sialoglycoprotein alpha; MN sialoglycoprotein
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P02724
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Expression Region
Leu20~Glu91
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Molecular Weight
15kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
The study of GYPA (Glycophorin A) recombinant protein has gained significance due to its crucial role in erythrocyte biology and immunology. GYPA, a sialoglycoprotein predominantly found on the surface of human red blood cells, is involved in several physiological processes, including cellular interaction, immune response, and maintaining red blood cell integrity. Research into GYPA is particularly pertinent in the context of blood transfusions, as it is a key antigen in the M/N blood group system, influencing compatibility and potential transfusion reactions. Additionally, GYPA serves as a model for studying membrane proteins and their functionalities, making it a valuable tool in biochemistry and molecular biology. The production of recombinant GYPA facilitates investigations into its structure-function relationships, aiding the development of therapies for various hematological disorders. Overall, the recombinant expression and characterization of GYPA not only enhance our understanding of its biological significance but also contribute to advancements in transfusion medicine and biopharmaceuticals.











